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Conserved domains on  [gi|4503649|ref|NP_000124|]
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coagulation factor IX isoform 1 preproprotein [Homo sapiens]

Protein Classification

coagulation factor( domain architecture ID 10637862)

coagulation factor is a vitamin K-dependent protein S1 family serine peptidase, similar to human coagulation factor X that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 227-457 1.82e-98

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 294.95  E-value: 1.82e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  227 VVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVE--TGVKITVVAGEHNIEETEHTEQKRNVIRIIPHH 303
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  304 NYNAAInkYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGS-GYVSGWGRVFHKGRSALVLQYLRVPLVDRATC 382
Cdd:cd00190  81 NYNPST--YDNDIALLKLKRPVTLSDNVRPICLPSSGYN---LPAGTtCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503649  383 LR--STKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEK 457
Cdd:cd00190 156 KRaySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 28-92 2.36e-29

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


:

Pssm-ID: 214503  Cd Length: 65  Bit Score: 109.32  E-value: 2.36e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503649      28 CTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV 92
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 93-129 5.80e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.18  E-value: 5.80e-10
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4503649   93 DGDQCES-NPCLNGGSCKDDINSYECWCPFGFEGKNCE 129
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 134-170 2.20e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.93  E-value: 2.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4503649    134 CNIKNGRCEQFCKNSAdNKVVCSCTEGYRLAENQKSC 170
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 227-457 1.82e-98

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 294.95  E-value: 1.82e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  227 VVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVE--TGVKITVVAGEHNIEETEHTEQKRNVIRIIPHH 303
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  304 NYNAAInkYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGS-GYVSGWGRVFHKGRSALVLQYLRVPLVDRATC 382
Cdd:cd00190  81 NYNPST--YDNDIALLKLKRPVTLSDNVRPICLPSSGYN---LPAGTtCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503649  383 LR--STKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEK 457
Cdd:cd00190 156 KRaySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 226-454 4.02e-94

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 283.80  E-value: 4.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649     226 RVVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVETGV--KITVVAGEHNIEETEHtEQKRNVIRIIPH 302
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSDpsNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649     303 HNYNAAInkYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGS-GYVSGWGRVFH-KGRSALVLQYLRVPLVDRA 380
Cdd:smart00020  80 PNYNPST--YDNDIALLKLKEPVTLSDNVRPICLPSSNYN---VPAGTtCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503649     381 TCLR--STKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVeGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWI 454
Cdd:smart00020 155 TCRRaySGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
227-454 7.04e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 244.27  E-value: 7.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649    227 VVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNY 305
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649    306 NAaiNKYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGSG-YVSGWGRVFHKGRSaLVLQYLRVPLVDRATCLR 384
Cdd:pfam00089  81 NP--DTLDNDIALLKLESPVTLGDTVRPICLPDASSD---LPVGTTcTVSGWGNTKTLGPS-DTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649    385 STKFTIYNNMFCAGFheGGRDSCQGDSGGPHVTEVEgtsFLTGIISWGEECAMKGKYGIYTKVSRYVNWI 454
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 225-458 1.20e-67

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.82  E-value: 1.20e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  225 TRVVGGEDAKPGQFPWQVVL---NGKVDAFCGGSIVNEKWIVTAAHCVETGV--KITVVAGEHNIEETEhtEQKRNVIRI 299
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSG--GTVVKVARI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  300 IPHHNYNAaiNKYNHDIALLELDEPLvlnSYVTPICIADkeyTNIFLKFGSGY-VSGWGRV-FHKGRSALVLQYLRVPLV 377
Cdd:COG5640 107 VVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLAT---SADAAAPGTPAtVAGWGRTsEGPGSQSGTLRKADVPVV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  378 DRATCLRSTKFtIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGE-ECAmKGKYGIYTKVSRYVNWIKE 456
Cdd:COG5640 179 SDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCA-AGYPGVYTRVSAYRDWIKS 256


                ..
gi 4503649  457 KT 458
Cdd:COG5640 257 TA 258
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 28-92 2.36e-29

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 109.32  E-value: 2.36e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503649      28 CTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV 92
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 52-92 3.38e-24

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 94.52  E-value: 3.38e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 4503649     52 LEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV 92
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 93-129 5.80e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.18  E-value: 5.80e-10
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4503649   93 DGDQCES-NPCLNGGSCKDDINSYECWCPFGFEGKNCE 129
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 134-170 2.20e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.93  E-value: 2.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4503649    134 CNIKNGRCEQFCKNSAdNKVVCSCTEGYRLAENQKSC 170
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
93-129 1.06e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.01  E-value: 1.06e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4503649      93 DGDQCES-NPCLNGGSCKDDINSYECWCPFGFE-GKNCE 129
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 97-127 2.06e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.21  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4503649     97 CESNPCLNGGSCKDDINSYECWCPFGFEGKN 127
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 123-169 3.28e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 38.91  E-value: 3.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4503649  123 FEGKNCELDVTCNIKNGRCEQFCKNSAdNKVVCSCTEGYRLAENQKS 169
Cdd:cd01475 179 FQGKICVVPDLCATLSHVCQQVCISTP-GSYLCACTEGYALLEDNKT 224
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 227-457 1.82e-98

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 294.95  E-value: 1.82e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  227 VVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVE--TGVKITVVAGEHNIEETEHTEQKRNVIRIIPHH 303
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  304 NYNAAInkYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGS-GYVSGWGRVFHKGRSALVLQYLRVPLVDRATC 382
Cdd:cd00190  81 NYNPST--YDNDIALLKLKRPVTLSDNVRPICLPSSGYN---LPAGTtCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503649  383 LR--STKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEK 457
Cdd:cd00190 156 KRaySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 226-454 4.02e-94

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 283.80  E-value: 4.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649     226 RVVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVETGV--KITVVAGEHNIEETEHtEQKRNVIRIIPH 302
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSDpsNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649     303 HNYNAAInkYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGS-GYVSGWGRVFH-KGRSALVLQYLRVPLVDRA 380
Cdd:smart00020  80 PNYNPST--YDNDIALLKLKEPVTLSDNVRPICLPSSNYN---VPAGTtCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503649     381 TCLR--STKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVeGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWI 454
Cdd:smart00020 155 TCRRaySGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
227-454 7.04e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 244.27  E-value: 7.04e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649    227 VVGGEDAKPGQFPWQVVL-NGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNY 305
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649    306 NAaiNKYNHDIALLELDEPLVLNSYVTPICIADKEYTnifLKFGSG-YVSGWGRVFHKGRSaLVLQYLRVPLVDRATCLR 384
Cdd:pfam00089  81 NP--DTLDNDIALLKLESPVTLGDTVRPICLPDASSD---LPVGTTcTVSGWGNTKTLGPS-DTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649    385 STKFTIYNNMFCAGFheGGRDSCQGDSGGPHVTEVEgtsFLTGIISWGEECAMKGKYGIYTKVSRYVNWI 454
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 225-458 1.20e-67

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.82  E-value: 1.20e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  225 TRVVGGEDAKPGQFPWQVVL---NGKVDAFCGGSIVNEKWIVTAAHCVETGV--KITVVAGEHNIEETEhtEQKRNVIRI 299
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSG--GTVVKVARI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  300 IPHHNYNAaiNKYNHDIALLELDEPLvlnSYVTPICIADkeyTNIFLKFGSGY-VSGWGRV-FHKGRSALVLQYLRVPLV 377
Cdd:COG5640 107 VVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLAT---SADAAAPGTPAtVAGWGRTsEGPGSQSGTLRKADVPVV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  378 DRATCLRSTKFtIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGE-ECAmKGKYGIYTKVSRYVNWIKE 456
Cdd:COG5640 179 SDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCA-AGYPGVYTRVSAYRDWIKS 256


                ..
gi 4503649  457 KT 458
Cdd:COG5640 257 TA 258
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 28-92 2.36e-29

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 109.32  E-value: 2.36e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503649      28 CTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV 92
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 52-92 3.38e-24

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 94.52  E-value: 3.38e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 4503649     52 LEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYV 92
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 243-454 1.39e-10

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.46  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  243 VLNGKVDAFCGGSIVNEKWIVTAAHCVETG------VKITVVAGEHNIEETEHTeqkrnVIRIIPHHNYNAAINkYNHDI 316
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGagggwaTNIVFVPGYNGGPYGTAT-----ATRFRVPPGWVASGD-AGYDY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503649  317 ALLELDEPLvlnsyvtpiciadkeyTNIFLKFGSGYVSGWGRvfhkGRSALVLQY-----LRVPLVDRATCLRSTKFTIY 391
Cdd:COG3591  79 ALLRLDEPL----------------GDTTGWLGLAFNDAPLA----GEPVTIIGYpgdrpKDLSLDCSGRVTGVQGNRLS 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503649  392 nnMFCagfheggrDSCQGDSGGPHVTEVEGTSFLTGIISWG-EECAMKGKYGIYTKVSRYVNWI 454
Cdd:COG3591 139 --YDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAGgADRANTGVRLTSAIVAALRAWA 192
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 93-129 5.80e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 54.18  E-value: 5.80e-10
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4503649   93 DGDQCES-NPCLNGGSCKDDINSYECWCPFGFEGKNCE 129
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 134-170 2.20e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.93  E-value: 2.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 4503649    134 CNIKNGRCEQFCKNSAdNKVVCSCTEGYRLAENQKSC 170
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
93-129 1.06e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.01  E-value: 1.06e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4503649      93 DGDQCES-NPCLNGGSCKDDINSYECWCPFGFE-GKNCE 129
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 98-129 7.03e-06

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 42.85  E-value: 7.03e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 4503649   98 ESNPCLNGGSCKDDINSYECWCPFGFEG-KNCE 129
Cdd:cd00053   4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 97-127 2.06e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.21  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4503649     97 CESNPCLNGGSCKDDINSYECWCPFGFEGKN 127
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 123-169 3.28e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 38.91  E-value: 3.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4503649  123 FEGKNCELDVTCNIKNGRCEQFCKNSAdNKVVCSCTEGYRLAENQKS 169
Cdd:cd01475 179 FQGKICVVPDLCATLSHVCQQVCISTP-GSYLCACTEGYALLEDNKT 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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